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In molecular biology, palmitoylation is the covalent attachment of fatty acids, such as palmitic acid, to cysteine (S-palmitoylation) and less frequently to serine and threonine (O-palmitoylation) residues of proteins, which are typically membrane proteins. [2] The precise function of palmitoylation depends on the particular protein being ...
The University of Minnesota Pathway Prediction System (UM-PPS) is a web tool that recognizes functional groups in organic compounds that are potential targets of microbial catabolic reactions and predicts transformations of these groups based on biotransformation rules. Multi-level predictions are made. (bio.tools entry) [116]
Some members of the family such as ZDHHC3 and ZDHHC7 enhance palmitoylation of proteins such as PSD-95, SNAP-25, GAP43, Gαs. Others such as ZDHHC9 showed specificity only toward the H-Ras protein. [3] However, a recent study questions the involvement of classical enzyme-substrate recognition and specificity in the palmitoylation reaction. [4]
Name Method description Type Link Initial release RaptorX-SS8 : predict both 3-state and 8-state secondary structure using conditional neural fields from PSI-BLAST profiles ...
Constituent amino-acids can be analyzed to predict secondary, tertiary and quaternary protein structure. This list of protein structure prediction software summarizes notable used software tools in protein structure prediction, including homology modeling, protein threading, ab initio methods, secondary structure prediction, and transmembrane helix and signal peptide prediction.
Prediction of 'aggregation-prone' in protein sequences, based on an aggregation propensity scale for natural amino acids derived from in vivo experiments. sequence - Overall aggregation and amyloidogenic regions Salsa [9] 2007 Web server - AMYPdb [10] Phenomenological
In palmitoleoylation, a palmitoleoyl group (derived from palmitoleic acid, pictured above) is added.. Palmitoleoylation is type of protein lipidation where the monounsaturated fatty acid palmitoleic acid is covalently attached to serine or threonine residues of proteins.
The protein palmitoylation is a reversible process. The addition of palmitoyl group increase the membrane association of the substrate protein while the removal by palmitoyl thioesterase decreases the membrane association.